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Results: 1-10 |
Results: 10
Buffer-anion-dependent Ca2+ leaching from horseradish peroxidase at low pH
Authors: Wright, PJ English, AM
Citation: Pj. Wright et Am. English, Buffer-anion-dependent Ca2+ leaching from horseradish peroxidase at low pH, J BIOL I CH, 6(4), 2001, pp. 348-358
Effects of metal ions on the oxidation and nitrosation of cysteine residues in proteins and enzymes
Authors: English, AM Wilcox, DE
Citation: Am. English et De. Wilcox, Effects of metal ions on the oxidation and nitrosation of cysteine residues in proteins and enzymes, METAL IONS, 38, 2001, pp. 313-350
Mass spectral analysis of protein-based radicals using DBNBS - Nonradical adduct formation versus spin trapping
Authors: Filosa, A English, AM
Citation: A. Filosa et Am. English, Mass spectral analysis of protein-based radicals using DBNBS - Nonradical adduct formation versus spin trapping, J BIOL CHEM, 276(24), 2001, pp. 21022-21027
Thermodynamic analysis of the binding of aromatic hydroxamic acid analogues to ferric horseradish peroxidase
Authors: Aitken, SM Turnbull, JL Percival, MD English, AM
Citation: Sm. Aitken et al., Thermodynamic analysis of the binding of aromatic hydroxamic acid analogues to ferric horseradish peroxidase, BIOCHEM, 40(46), 2001, pp. 13980-13989
Two-dimensional infrared correlation spectroscopy as a probe of sequentialevents in the thermal unfolding of cytochromes c
Authors: Filosa, A Wang, Y Ismail, A English, AM
Citation: A. Filosa et al., Two-dimensional infrared correlation spectroscopy as a probe of sequentialevents in the thermal unfolding of cytochromes c, BIOCHEM, 40(28), 2001, pp. 8256-8263
Metal chelators inhibit S-nitrosation of Cys beta 93 in oxyhemoglobin
Authors: Romeo, AA Filosa, A Capobianco, JA English, AM
Citation: Aa. Romeo et al., Metal chelators inhibit S-nitrosation of Cys beta 93 in oxyhemoglobin, J AM CHEM S, 123(8), 2001, pp. 1782-1783
Probing local thermal stabilities of bovine, horse, and tuna ferricytochromes c at pH 7
Authors: Filosa, A English, AM
Citation: A. Filosa et Am. English, Probing local thermal stabilities of bovine, horse, and tuna ferricytochromes c at pH 7, J BIOL I CH, 5(4), 2000, pp. 448-454
Influence of protein environment on magnetic circular dichroism spectral properties of ferric and ferrous ligand complexes of yeast cytochrome c peroxidase
Authors: Pond, AE Sono, M Elenkova, EA Goodin, DB English, AM Dawson, JH
Citation: Ae. Pond et al., Influence of protein environment on magnetic circular dichroism spectral properties of ferric and ferrous ligand complexes of yeast cytochrome c peroxidase, BIOSPECTROS, 5(5), 1999, pp. S42-S52
FTIR-monitored thermal titration reveals different mechanisms for the alkaline isomerization of tuna compared to horse and bovine cytochromes c
Authors: Filosa, A Ismail, AA English, AM
Citation: A. Filosa et al., FTIR-monitored thermal titration reveals different mechanisms for the alkaline isomerization of tuna compared to horse and bovine cytochromes c, J BIOL I CH, 4(6), 1999, pp. 717-726
Magnetic circular dichroism studies of the active site heme coordination sphere of exogenous ligand-free ferric cytochrome c peroxidase from yeast: effects of sample history and pH
Authors: Pond, AE Sono, M Elenkova, EA McRee, DE Goodin, DB English, AM Dawson, JH
Citation: Ae. Pond et al., Magnetic circular dichroism studies of the active site heme coordination sphere of exogenous ligand-free ferric cytochrome c peroxidase from yeast: effects of sample history and pH, J INORG BIO, 76(3-4), 1999, pp. 165-174
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